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Association of suppression of extracellular signal-regulated kinase phosphorylation by epigallocatechin gallate with the reduction of matrix metalloproteinase activities in human fibrosarcoma HT1080 cells.
J Agric Food Chem 2003; 51(7):1858-63JA

Abstract

Matrix metalloproteinases (MMPs) play a crucial role in the process of cancer invasion and metastasis. Previous findings suggested that epigallocatechin gallate (EGCG), a main flavanol of green tea, caused decreased levels of MMP-2 and MMP-9 activities to be secreted into culture medium. To obtain further information on EGCG-mediated regulation of these MMPs, the effects of EGCG on enzyme activity, mRNA expression, and mitogen-activated protein kinase (MAPK) activities in human fibrosarcoma HT1080 cells were examined. EGCG was confirmed to suppress the gelatin-degrading activities due to MMP-2 and MMP-9 in the culture medium. This suppression of enzyme activities by EGCG was consistent with the decreased levels of MMP-2 and MMP-9 mRNAs. EGCG-mediated suppression was also observed for MT1-MMP mRNA. EGCG-mediated suppression of the level of MMP-9 transcript was correlated with its suppression of MMP-9 promoter activity. EGCG inhibited the phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), which are the members of an MAPK family necessary for MMP-9 up-regulation. EGCG also suppressed p38 MAPK activity but gave no effects on stress-activated protein kinase/c-Jun N-terminal kinase activity. These findings suggest that suppression of ERK phosphorylation by EGCG is involved in the inhibition of expression for MMP-2 and MMP-9 mRNAs, leading to the reduction of their enzyme activities of the cancer cells. Methyl derivatives, epigallocatechin-3-O-(3-O-methyl) gallate and epigallocatechin-3-O-(4-O-methyl) gallate, exhibited effects similar to, but weaker than, those of EGCG, suggesting the important role of an unsubstituted triphenolic ester structure in these activities.

Authors+Show Affiliations

National Institute of Vegetable and Tea Science, NARO, 2769 Kanaya, Shizuoka 428-8501, Japan. marimy@affrc.go.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12643642

Citation

Maeda-Yamamoto, Mari, et al. "Association of Suppression of Extracellular Signal-regulated Kinase Phosphorylation By Epigallocatechin Gallate With the Reduction of Matrix Metalloproteinase Activities in Human Fibrosarcoma HT1080 Cells." Journal of Agricultural and Food Chemistry, vol. 51, no. 7, 2003, pp. 1858-63.
Maeda-Yamamoto M, Suzuki N, Sawai Y, et al. Association of suppression of extracellular signal-regulated kinase phosphorylation by epigallocatechin gallate with the reduction of matrix metalloproteinase activities in human fibrosarcoma HT1080 cells. J Agric Food Chem. 2003;51(7):1858-63.
Maeda-Yamamoto, M., Suzuki, N., Sawai, Y., Miyase, T., Sano, M., Hashimoto-Ohta, A., & Isemura, M. (2003). Association of suppression of extracellular signal-regulated kinase phosphorylation by epigallocatechin gallate with the reduction of matrix metalloproteinase activities in human fibrosarcoma HT1080 cells. Journal of Agricultural and Food Chemistry, 51(7), pp. 1858-63.
Maeda-Yamamoto M, et al. Association of Suppression of Extracellular Signal-regulated Kinase Phosphorylation By Epigallocatechin Gallate With the Reduction of Matrix Metalloproteinase Activities in Human Fibrosarcoma HT1080 Cells. J Agric Food Chem. 2003 Mar 26;51(7):1858-63. PubMed PMID: 12643642.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Association of suppression of extracellular signal-regulated kinase phosphorylation by epigallocatechin gallate with the reduction of matrix metalloproteinase activities in human fibrosarcoma HT1080 cells. AU - Maeda-Yamamoto,Mari, AU - Suzuki,Naoko, AU - Sawai,Yoshinori, AU - Miyase,Toshio, AU - Sano,Mitsuaki, AU - Hashimoto-Ohta,Akiko, AU - Isemura,Mamoru, PY - 2003/3/20/pubmed PY - 2003/5/8/medline PY - 2003/3/20/entrez SP - 1858 EP - 63 JF - Journal of agricultural and food chemistry JO - J. Agric. Food Chem. VL - 51 IS - 7 N2 - Matrix metalloproteinases (MMPs) play a crucial role in the process of cancer invasion and metastasis. Previous findings suggested that epigallocatechin gallate (EGCG), a main flavanol of green tea, caused decreased levels of MMP-2 and MMP-9 activities to be secreted into culture medium. To obtain further information on EGCG-mediated regulation of these MMPs, the effects of EGCG on enzyme activity, mRNA expression, and mitogen-activated protein kinase (MAPK) activities in human fibrosarcoma HT1080 cells were examined. EGCG was confirmed to suppress the gelatin-degrading activities due to MMP-2 and MMP-9 in the culture medium. This suppression of enzyme activities by EGCG was consistent with the decreased levels of MMP-2 and MMP-9 mRNAs. EGCG-mediated suppression was also observed for MT1-MMP mRNA. EGCG-mediated suppression of the level of MMP-9 transcript was correlated with its suppression of MMP-9 promoter activity. EGCG inhibited the phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), which are the members of an MAPK family necessary for MMP-9 up-regulation. EGCG also suppressed p38 MAPK activity but gave no effects on stress-activated protein kinase/c-Jun N-terminal kinase activity. These findings suggest that suppression of ERK phosphorylation by EGCG is involved in the inhibition of expression for MMP-2 and MMP-9 mRNAs, leading to the reduction of their enzyme activities of the cancer cells. Methyl derivatives, epigallocatechin-3-O-(3-O-methyl) gallate and epigallocatechin-3-O-(4-O-methyl) gallate, exhibited effects similar to, but weaker than, those of EGCG, suggesting the important role of an unsubstituted triphenolic ester structure in these activities. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/12643642/Association_of_suppression_of_extracellular_signal_regulated_kinase_phosphorylation_by_epigallocatechin_gallate_with_the_reduction_of_matrix_metalloproteinase_activities_in_human_fibrosarcoma_HT1080_cells_ L2 - https://dx.doi.org/10.1021/jf021039l DB - PRIME DP - Unbound Medicine ER -